Recent progresses in studying helix-helix interactions in proteins by incorporating the wenxiang diagram into the NMR spectroscopy

Current Topics in Medicinal Chemistry

Volumn 16, Issue 6, 2016, Pages 581-590

  Zhou, Guo Ping ^a,c   Chen, Dong ^a   Liao, Siming ^a   Huang, Ri Bo ^a,b  

^a NATIONAL ENGINEERING RESEARCH CENTER FOR NON FOOD BIOREFINERY   (China)

^b GUANGXI UNIVERSITY   (China)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alpha helical stability; Hydrophilic residues; Hydrophobic residues; Leucine zipper coiled coil structure (LZCC); NMR spectroscopy; Protein misfolding; Protein protein interaction (PPI); Wenxiang diagram

Indexed keywords

AMINO ACID; LEUCINE ZIPPER PROTEIN; MYOSIN BINDING PROTEIN C; PEPTIDES AND PROTEINS; PROTEIN KINASE 1; UNCLASSIFIED DRUG; PROTEIN; PROTEIN BINDING;

AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; HELIX HELIX INTERACTION; HUMAN; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; VASCULAR SMOOTH MUSCLE CELL; WENXIANG DIAGRAM; ANIMAL; CHEMISTRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE;

AMINO ACIDS; ANIMALS; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 84962493098     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026615666150819104617     Document Type: Article

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